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An Ex vivo Assay to Study Candida albicans Hyphal Morphogenesis in the Gastrointestinal Tract
Published on: July 1, 2020
The 65 kDa mannoprotein gene of Candida albicans encodes a putative beta-glucanase adhesin required for hyphal
Silvia Sandini1, Roberto La Valle, Flavia De Bernardis
1Department of Infectious, Parasitic and Immuno-mediated Diseases, Instituto Superiore di Sanità, Rome, Italy.
Abstract:
Mannoproteins are fungal cell wall components which play a main role in host-parasite relationship. Camp65p is a putative beta-glucanase mannoprotein of 65 kDa which has been characterized as a main target of human immune response against Candida albicans. However, nothing is known about its specific contribution to the biology and virulence of this fungus. We constructed CAMP65 knock-out mutants including null camp65/camp65 and CAMP65/camp65 heterozygous strains. The null strains had the same growth rate and morphology under yeast form as the wild-type strain but they were severely affected in hyphal morphogenesis both in vitro and in vivo. Hyphae formation was restored in revertant strains. The null mutants lost adherence to the plastic, and this was in keeping with the strong inhibition of fungal cell adherence to plastic exerted by anti-Camp65p antibodies. The null mutants were also significantly less virulent than the parental strains, and this loss of virulence was observed both in systemic and in mucosal C. albicans infection models. Nonetheless, the virulence in both infectious models was regained by the CAMP65 revertants. Thus, CAMP65 of C. albicans encodes a putative beta-glucanase, mannoprotein adhesin, which has a dual role (hyphal cell wall construction and virulence), accounting for the particular relevance of host immune response against this mannoprotein.
Insights
Camp65p mannoprotein is crucial for Candida albicans virulence and hyphal development. Deleting CAMP65 impairs fungal adherence and infection models, highlighting its role in host-parasite interactions.
Area of Science:
- Mycology
- Immunology
- Molecular Biology
Background:
- Mannoproteins are key fungal cell wall components involved in host interactions.
- Camp65p is a 65 kDa mannoprotein and a target of human immune response against Candida albicans.
- The specific biological and virulence roles of Camp65p in C. albicans remain largely unknown.
Purpose of the Study:
- To investigate the function of CAMP65 in Candida albicans.
- To determine the contribution of Camp65p to fungal morphology, adherence, and virulence.
- To understand the relevance of Camp65p in the context of host immune response.
Main Methods:
- Construction and characterization of CAMP65 knock-out mutants (null and heterozygous).
- Assessment of fungal growth rate, morphology (yeast and hyphal forms), and adherence.
- Evaluation of virulence in systemic and mucosal infection models in vivo.
- Analysis of hyphal formation restoration in revertant strains.
Main Results:
- Null camp65/camp65 mutants exhibited normal yeast growth but were severely impaired in hyphal morphogenesis.
- CAMP65 deletion resulted in reduced fungal adherence to plastic, inhibited by anti-Camp65p antibodies.
- Null mutants showed significantly reduced virulence in both systemic and mucosal C. albicans infection models.
- Revertant strains restored both hyphal formation and virulence, confirming CAMP65's role.
Conclusions:
- CAMP65 encodes a mannoprotein with beta-glucanase and adhesin activities.
- Camp65p plays a dual role in hyphal cell wall construction and C. albicans virulence.
- The findings underscore the significance of Camp65p as a target for host immune responses against C. albicans infections.
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